The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes

Andrew W. Tanner, Valerie J. Carabetta, Ryan J. Martinie, Ameya A. Mashruwala, Jeffrey M. Boyd, Carsten Krebs, David Dubnau

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

During times of environmental insult, Bacillus subtilis undergoes developmental changes leading to biofilm formation, sporulation and competence. Each of these states is regulated in part by the phosphorylated form of the master response regulator Spo0A (Spo0A∼P). The phosphorylation state of Spo0A is controlled by a multi-component phosphorelay. RicA, RicF and RicT (previously YmcA, YlbF and YaaT) have been shown to be important regulatory proteins for multiple developmental fates. These proteins directly interact and form a stable complex, which has been proposed to accelerate the phosphorelay. Indeed, this complex is sufficient to stimulate the rate of phosphotransfer amongst the phosphorelay proteins in vitro. In this study, we demonstrate that two [4Fe-4S]2+ clusters can be assembled on the complex. As with other iron-sulfur cluster-binding proteins, the complex was also found to bind FAD, hinting that these cofactors may be involved in sensing the cellular redox state. This work provides the first comprehensive characterization of an iron-sulfur protein complex that regulates Spo0A∼P levels. Phylogenetic and genetic evidence suggests that the complex plays a broader role beyond stimulation of the phosphorelay.

Original languageEnglish (US)
Pages (from-to)837-850
Number of pages14
JournalMolecular Microbiology
Volume104
Issue number5
DOIs
StatePublished - Jun 1 2017

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Oxidation-Reduction
Iron-Sulfur Proteins
Proteins
Flavin-Adenine Dinucleotide
Biofilms
Bacillus subtilis
Sulfur
Mental Competency
Carrier Proteins
Iron
Phosphorylation
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Tanner, A. W., Carabetta, V. J., Martinie, R. J., Mashruwala, A. A., Boyd, J. M., Krebs, C., & Dubnau, D. (2017). The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes. Molecular Microbiology, 104(5), 837-850. https://doi.org/10.1111/mmi.13667
Tanner, Andrew W. ; Carabetta, Valerie J. ; Martinie, Ryan J. ; Mashruwala, Ameya A. ; Boyd, Jeffrey M. ; Krebs, Carsten ; Dubnau, David. / The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes. In: Molecular Microbiology. 2017 ; Vol. 104, No. 5. pp. 837-850.
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abstract = "During times of environmental insult, Bacillus subtilis undergoes developmental changes leading to biofilm formation, sporulation and competence. Each of these states is regulated in part by the phosphorylated form of the master response regulator Spo0A (Spo0A∼P). The phosphorylation state of Spo0A is controlled by a multi-component phosphorelay. RicA, RicF and RicT (previously YmcA, YlbF and YaaT) have been shown to be important regulatory proteins for multiple developmental fates. These proteins directly interact and form a stable complex, which has been proposed to accelerate the phosphorelay. Indeed, this complex is sufficient to stimulate the rate of phosphotransfer amongst the phosphorelay proteins in vitro. In this study, we demonstrate that two [4Fe-4S]2+ clusters can be assembled on the complex. As with other iron-sulfur cluster-binding proteins, the complex was also found to bind FAD, hinting that these cofactors may be involved in sensing the cellular redox state. This work provides the first comprehensive characterization of an iron-sulfur protein complex that regulates Spo0A∼P levels. Phylogenetic and genetic evidence suggests that the complex plays a broader role beyond stimulation of the phosphorelay.",
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Tanner, AW, Carabetta, VJ, Martinie, RJ, Mashruwala, AA, Boyd, JM, Krebs, C & Dubnau, D 2017, 'The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes', Molecular Microbiology, vol. 104, no. 5, pp. 837-850. https://doi.org/10.1111/mmi.13667

The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes. / Tanner, Andrew W.; Carabetta, Valerie J.; Martinie, Ryan J.; Mashruwala, Ameya A.; Boyd, Jeffrey M.; Krebs, Carsten; Dubnau, David.

In: Molecular Microbiology, Vol. 104, No. 5, 01.06.2017, p. 837-850.

Research output: Contribution to journalArticle

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T1 - The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes

AU - Tanner, Andrew W.

AU - Carabetta, Valerie J.

AU - Martinie, Ryan J.

AU - Mashruwala, Ameya A.

AU - Boyd, Jeffrey M.

AU - Krebs, Carsten

AU - Dubnau, David

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Y1 - 2017/6/1

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AB - During times of environmental insult, Bacillus subtilis undergoes developmental changes leading to biofilm formation, sporulation and competence. Each of these states is regulated in part by the phosphorylated form of the master response regulator Spo0A (Spo0A∼P). The phosphorylation state of Spo0A is controlled by a multi-component phosphorelay. RicA, RicF and RicT (previously YmcA, YlbF and YaaT) have been shown to be important regulatory proteins for multiple developmental fates. These proteins directly interact and form a stable complex, which has been proposed to accelerate the phosphorelay. Indeed, this complex is sufficient to stimulate the rate of phosphotransfer amongst the phosphorelay proteins in vitro. In this study, we demonstrate that two [4Fe-4S]2+ clusters can be assembled on the complex. As with other iron-sulfur cluster-binding proteins, the complex was also found to bind FAD, hinting that these cofactors may be involved in sensing the cellular redox state. This work provides the first comprehensive characterization of an iron-sulfur protein complex that regulates Spo0A∼P levels. Phylogenetic and genetic evidence suggests that the complex plays a broader role beyond stimulation of the phosphorelay.

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